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Mercury in PDB 1g0e: Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

Enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

All present enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole:
4.2.1.1;

Protein crystallography data

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e was solved by D.Duda, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.142, 41.490, 72.063, 90.00, 104.28, 90.00
R / Rfree (%) 17.9 / 20

Other elements in 1g0e:

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole (pdb code 1g0e). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e:

Mercury binding site 1 out of 1 in 1g0e

Go back to Mercury Binding Sites List in 1g0e
Mercury binding site 1 out of 1 in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:12.1
occ:1.00
SG A:CYS206 2.3 8.8 1.0
O A:HOH271 2.4 14.4 1.0
O A:GLN137 2.9 6.2 1.0
CB A:CYS206 2.9 6.3 1.0
O A:GLU205 3.2 5.3 1.0
O A:VAL135 3.3 10.1 1.0
C A:GLN137 3.4 7.2 1.0
O A:HOH375 3.5 18.8 1.0
O A:HOH374 3.5 26.4 1.0
CA A:CYS206 3.5 4.5 1.0
C A:GLU205 3.5 4.8 1.0
N A:GLN137 3.7 8.8 1.0
N A:CYS206 3.7 4.7 1.0
C A:VAL135 3.8 9.2 1.0
C A:GLN136 4.0 9.5 1.0
N A:PRO138 4.1 6.8 1.0
CA A:GLN137 4.1 7.5 1.0
CA A:PRO138 4.3 6.4 1.0
N A:GLN136 4.3 9.9 1.0
CA A:GLN136 4.3 10.5 1.0
N A:GLU205 4.3 4.8 1.0
O A:HOH369 4.5 16.2 1.0
CA A:GLU205 4.5 4.8 1.0
O A:GLN136 4.6 9.7 1.0
CA A:VAL135 4.6 8.7 1.0
CB A:LEU204 4.7 5.7 1.0
O A:ALA134 4.9 7.2 1.0
C A:LEU204 4.9 4.9 1.0
C A:CYS206 5.0 4.1 1.0

Reference:

D.Duda, C.Tu, M.Qian, P.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II. Biochemistry V. 40 1741 2001.
ISSN: ISSN 0006-2960
PubMed: 11327835
DOI: 10.1021/BI002295Z
Page generated: Wed Oct 28 18:39:18 2020

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